CATB_PIG
ID CATB_PIG Reviewed; 335 AA.
AC A1E295;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Cathepsin B;
DE EC=3.4.22.1 {ECO:0000250|UniProtKB:P07858};
DE Contains:
DE RecName: Full=Cathepsin B light chain {ECO:0000250|UniProtKB:P07858};
DE Contains:
DE RecName: Full=Cathepsin B heavy chain {ECO:0000250|UniProtKB:P07858};
DE Flags: Precursor;
GN Name=CTSB;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chen L., Li X.W., Zhu L., Li Q., Li M.Z.;
RT "Molecular cloning and polymorphism of cathepsin B (CTSB) gene in
RT porcine.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22261194; DOI=10.1161/circulationaha.111.056952;
RA Barallobre-Barreiro J., Didangelos A., Schoendube F.A., Drozdov I., Yin X.,
RA Fernandez-Caggiano M., Willeit P., Puntmann V.O., Aldama-Lopez G.,
RA Shah A.M., Domenech N., Mayr M.;
RT "Proteomics analysis of cardiac extracellular matrix remodeling in a
RT porcine model of ischemia/reperfusion injury.";
RL Circulation 125:789-802(2012).
CC -!- FUNCTION: Thiol protease which is believed to participate in
CC intracellular degradation and turnover of proteins (By similarity).
CC Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity).
CC Involved in the solubilization of cross-linked TG/thyroglobulin in the
CC thyroid follicle lumen (By similarity). Has also been implicated in
CC tumor invasion and metastasis (By similarity).
CC {ECO:0000250|UniProtKB:P00787, ECO:0000250|UniProtKB:P07858,
CC ECO:0000250|UniProtKB:P10605}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity for peptide
CC bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule
CC substrates (thus differing from cathepsin L). In addition to being an
CC endopeptidase, shows peptidyl-dipeptidase activity, liberating C-
CC terminal dipeptides.; EC=3.4.22.1;
CC Evidence={ECO:0000250|UniProtKB:P07858};
CC -!- SUBUNIT: Dimer of a heavy chain and a light chain cross-linked by a
CC disulfide bond. Interacts with SRPX2. Directly interacts with SHKBP1.
CC {ECO:0000250|UniProtKB:P07858}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P07858}.
CC Melanosome {ECO:0000250|UniProtKB:P07858}. Secreted, extracellular
CC space {ECO:0000269|PubMed:22261194}. Apical cell membrane
CC {ECO:0000250|UniProtKB:P10605}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P10605}; Extracellular side
CC {ECO:0000250|UniProtKB:P10605}. Note=Localizes to the lumen of thyroid
CC follicles and to the apical membrane of thyroid epithelial cells.
CC {ECO:0000250|UniProtKB:P10605}.
CC -!- TISSUE SPECIFICITY: Expressed in heart (at protein level).
CC {ECO:0000269|PubMed:22261194}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR EMBL; EF095956; ABK96810.1; -; mRNA.
DR RefSeq; NP_001090927.1; NM_001097458.1.
DR RefSeq; XP_005657322.2; XM_005657265.2.
DR RefSeq; XP_005657323.1; XM_005657266.2.
DR RefSeq; XP_005657324.1; XM_005657267.2.
DR RefSeq; XP_013845747.1; XM_013990293.1.
DR AlphaFoldDB; A1E295; -.
DR SMR; A1E295; -.
DR IntAct; A1E295; 2.
DR STRING; 9823.ENSSSCP00000024395; -.
DR MEROPS; C01.060; -.
DR PaxDb; A1E295; -.
DR PeptideAtlas; A1E295; -.
DR PRIDE; A1E295; -.
DR Ensembl; ENSSSCT00000049406; ENSSSCP00000046743; ENSSSCG00000023666.
DR Ensembl; ENSSSCT00015003893; ENSSSCP00015001345; ENSSSCG00015002579.
DR Ensembl; ENSSSCT00015003921; ENSSSCP00015001359; ENSSSCG00015002579.
DR Ensembl; ENSSSCT00025035776; ENSSSCP00025014937; ENSSSCG00025026366.
DR Ensembl; ENSSSCT00030004003; ENSSSCP00030001587; ENSSSCG00030002799.
DR Ensembl; ENSSSCT00035095352; ENSSSCP00035040101; ENSSSCG00035070519.
DR Ensembl; ENSSSCT00040104061; ENSSSCP00040047304; ENSSSCG00040075101.
DR Ensembl; ENSSSCT00045032170; ENSSSCP00045022270; ENSSSCG00045018627.
DR Ensembl; ENSSSCT00045032247; ENSSSCP00045022327; ENSSSCG00045018627.
DR Ensembl; ENSSSCT00045032316; ENSSSCP00045022379; ENSSSCG00045018627.
DR Ensembl; ENSSSCT00045032398; ENSSSCP00045022441; ENSSSCG00045018627.
DR Ensembl; ENSSSCT00045032468; ENSSSCP00045022486; ENSSSCG00045018627.
DR Ensembl; ENSSSCT00050073267; ENSSSCP00050031547; ENSSSCG00050053741.
DR Ensembl; ENSSSCT00055000049; ENSSSCP00055000041; ENSSSCG00055000027.
DR Ensembl; ENSSSCT00060041735; ENSSSCP00060017740; ENSSSCG00060030710.
DR Ensembl; ENSSSCT00065036005; ENSSSCP00065015077; ENSSSCG00065026769.
DR Ensembl; ENSSSCT00065036011; ENSSSCP00065015080; ENSSSCG00065026769.
DR Ensembl; ENSSSCT00065036014; ENSSSCP00065015082; ENSSSCG00065026769.
DR Ensembl; ENSSSCT00065036024; ENSSSCP00065015086; ENSSSCG00065026769.
DR GeneID; 100037961; -.
DR KEGG; ssc:100037961; -.
DR CTD; 1508; -.
DR VGNC; VGNC:87074; CTSB.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000158680; -.
DR HOGENOM; CLU_012184_3_3_1; -.
DR InParanoid; A1E295; -.
DR OrthoDB; 865289at2759; -.
DR TreeFam; TF314576; -.
DR Reactome; R-SSC-1442490; Collagen degradation.
DR Reactome; R-SSC-1679131; Trafficking and processing of endosomal TLR.
DR Reactome; R-SSC-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-SSC-2132295; MHC class II antigen presentation.
DR Reactome; R-SSC-6798695; Neutrophil degranulation.
DR Proteomes; UP000008227; Chromosome 14.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000023666; Expressed in adult mammalian kidney and 43 other tissues.
DR ExpressionAtlas; A1E295; baseline and differential.
DR Genevisible; A1E295; SS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR012599; Propeptide_C1A.
DR Pfam; PF00112; Peptidase_C1; 1.
DR Pfam; PF08127; Propeptide_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Disulfide bond; Glycoprotein; Hydrolase;
KW Lysosome; Membrane; Protease; Reference proteome; Secreted; Signal;
KW Thiol protease; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..79
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT /id="PRO_0000330885"
FT CHAIN 80..332
FT /note="Cathepsin B"
FT /id="PRO_0000330886"
FT CHAIN 80..126
FT /note="Cathepsin B light chain"
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT /id="PRO_0000330887"
FT CHAIN 129..332
FT /note="Cathepsin B heavy chain"
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT /id="PRO_0000330888"
FT PROPEP 333..335
FT /evidence="ECO:0000250|UniProtKB:P07688"
FT /id="PRO_0000330889"
FT ACT_SITE 108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT ACT_SITE 278
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 298
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT MOD_RES 220
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10605"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P07688"
FT DISULFID 93..122
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 105..150
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 141..207
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 142..146
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 179..211
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 187..198
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 227..331
FT /evidence="ECO:0000250|UniProtKB:P07858"
SQ SEQUENCE 335 AA; 36901 MW; D94E13E44822C19D CRC64;
MWRLLATLSC LVLLTSARES LHFQPLSDEL VNFINKQNTT WTAGHNFYNV DLSYVKKLCG
TFLGGPKLPQ RAAFAADMIL PKSFDAREQW PNCPTIKEIR DQGSCGSCWA FGAVEAISDR
ICIRSNGRVN VEVSAEDMLT CCGDECGDGC NGGFPSGAWN FWTKKGLVSG GLYDSHVGCR
PYSIPPCEHH VNGSRPPCTG EGDTPKCSKI CEPGYTPSYK EDKHFGCSSY SISRNEKEIM
AEIYKNGPVE GAFTVYSDFL QYKSGVYQHV TGDLMGGHAI RILGWGVENG TPYWLVGNSW
NTDWGDNGFF KILRGQDHCG IESEIVAGIP CTPHF
